1TWZ
Dihydropteroate Synthetase, With Bound Substrate Analogue PtP, From Bacillus anthracis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004156 | molecular_function | dihydropteroate synthase activity |
| A | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042558 | biological_process | pteridine-containing compound metabolic process |
| A | 0044237 | biological_process | cellular metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004156 | molecular_function | dihydropteroate synthase activity |
| B | 0009396 | biological_process | folic acid-containing compound biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042558 | biological_process | pteridine-containing compound metabolic process |
| B | 0044237 | biological_process | cellular metabolic process |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046656 | biological_process | folic acid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 278 |
| Chain | Residue |
| B | LYS50 |
| B | ARG53 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 278 |
| Chain | Residue |
| A | LYS50 |
| A | ARG53 |
| A | HOH307 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 279 |
| Chain | Residue |
| A | ASN27 |
| A | ARG219 |
| A | HOH296 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 279 |
| Chain | Residue |
| B | ARG219 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 280 |
| Chain | Residue |
| B | SER221 |
| B | ARG234 |
| B | HOH306 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 280 |
| Chain | Residue |
| A | SER221 |
| A | ARG234 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 281 |
| Chain | Residue |
| A | GLU198 |
| A | ARG201 |
| A | ASN202 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 281 |
| Chain | Residue |
| B | ARG201 |
| B | ASN202 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PMM A 282 |
| Chain | Residue |
| A | ASP101 |
| A | ASN120 |
| A | ILE122 |
| A | MET145 |
| A | ASP184 |
| A | PHE189 |
| A | GLY216 |
| A | LYS220 |
| A | ARG254 |
| A | HOH316 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PMM B 282 |
| Chain | Residue |
| B | ASP101 |
| B | ASN120 |
| B | ILE122 |
| B | MET145 |
| B | ASP184 |
| B | PHE189 |
| B | GLY216 |
| B | LYS220 |
| B | ARG254 |
| B | HIS256 |
| B | HOH292 |
Functional Information from PROSITE/UniProt
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aj0 |
| Chain | Residue | Details |
| A | ARG254 | |
| A | ASN27 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1aj0 |
| Chain | Residue | Details |
| B | ARG254 | |
| B | ASN27 |
